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PDBsum entry 5jyh
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DOI no:
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Febs Lett
590:2286-2296
(2016)
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PubMed id:
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Solution structure and antiparasitic activity of scorpine-like peptides from Hoffmannihadrurus gertschi.
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D.Flores-Solis,
Y.Toledano,
O.Rodríguez-Lima,
P.Cano-Sánchez,
B.E.Ramírez-Cordero,
A.Landa,
R.C.Rodríguez de la Vega,
F.Del Rio-Portilla.
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ABSTRACT
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Scorpine-like peptides are two domain peptides found in different scorpion
venoms displaying various antimicrobial, cytolytic, and potassium
channel-blocking activities. The relative contribution of each domain to their
different activities remains to be elucidated. Here, we report the recombinant
production, solution structure, and antiparasitic activity of Hge36, first
identified as a naturally occurring truncated form of a Scorpine-like peptide
from the venom of Hoffmannihadrurus gertschi. We also show that removing the
first four residues from Hge36 renders a molecule with enhanced potassium
channel-blocking and antiparasitic activities. Our results are important to
rationalize the structure-function relationships of a pharmacologically
versatile molecular scaffold.
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}
}
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